ID N4UI86_FUSC1 Unreviewed; 732 AA.
AC N4UI86;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA-binding protein RAP1 {ECO:0000256|RuleBase:RU367107};
GN ORFNames=FOC1_g10012108 {ECO:0000313|EMBL:ENH69750.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH69750.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
CC -!- FUNCTION: Involved in the regulation of telomere length, clustering and
CC has a specific role in telomere position effect (TPE).
CC {ECO:0000256|RuleBase:RU367107}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367107}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU367107}.
CC Chromosome, telomere {ECO:0000256|RuleBase:RU367107}.
CC -!- SIMILARITY: Belongs to the RAP1 family. {ECO:0000256|ARBA:ARBA00010467,
CC ECO:0000256|RuleBase:RU367107}.
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DR EMBL; KB730216; ENH69750.1; -; Genomic_DNA.
DR AlphaFoldDB; N4UI86; -.
DR STRING; 1229664.N4UI86; -.
DR VEuPathDB; FungiDB:FOC1_g10012108; -.
DR HOGENOM; CLU_006783_1_0_1; -.
DR OMA; WKYITDS; -.
DR Proteomes; UP000016928; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IEA:UniProtKB-UniRule.
DR CDD; cd16100; ARID; 1.
DR CDD; cd11655; rap1_myb-like; 1.
DR Gene3D; 1.10.10.2170; -; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR021661; Rap1_C.
DR InterPro; IPR038104; Rap1_C_sf.
DR InterPro; IPR015010; Rap1_Myb_dom.
DR InterPro; IPR039595; TE2IP/Rap1.
DR PANTHER; PTHR16466; TELOMERE REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR PANTHER; PTHR16466:SF6; TELOMERIC REPEAT-BINDING FACTOR 2-INTERACTING PROTEIN 1; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF16589; BRCT_2; 1.
DR Pfam; PF08914; Myb_DNA-bind_2; 1.
DR Pfam; PF11626; Rap1_C; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU367107};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367107};
KW Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW Telomere {ECO:0000256|ARBA:ARBA00022895, ECO:0000256|RuleBase:RU367107};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 17..90
FT /note="BRCT"
FT /evidence="ECO:0000259|Pfam:PF16589"
FT DOMAIN 113..172
FT /note="Rap1 Myb"
FT /evidence="ECO:0000259|Pfam:PF08914"
FT DOMAIN 275..356
FT /note="ARID"
FT /evidence="ECO:0000259|Pfam:PF01388"
FT DOMAIN 617..720
FT /note="TRF2-interacting telomeric protein/Rap1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11626"
FT REGION 96..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 83323 MW; 6473AE02A8850915 CRC64;
MPPAVTYDGV EGAEGGTIFK DRKFWLSHRV PMRNRWTELI TQNGGKVVML EKHADMLIAD
HLRKKDAPPG SYSWKFIEDS VKNGYIQIKD KYLIGRHPDE PRPVGSNQAK KSTRTKFTAE
DDAKLTRWAL NHPDEQKGNQ IWYEYERINP RHTAQSWRDH WIKKLQFLDR KKLESMAASA
PAEAGPVAST SENTAEDHST VIRVPRKAAV QRAPAQRVNN QVDAGPIRRA PQPQPTTVPS
QGPREANKPR PSIEDGQEEE EQEQEQEALA LLRYNWYQDL DEYIKVTERD IKRNLNINGK
KIELFDLMLA ARDAPVSQDS QLTDWYRVAE NLGFVEPDQH TVNELHLCYE ENLMDFLEIM
ESFEVNSEDA GPESQGAAPD MDPSQDIDFE DGQERGLLQS QVPSSPPIAA SSLKRTAGEP
PLASPERFKK RRYSKDMEIP STPDAEETSK LQRAQETSPG ALRTSQWLGY IGESEASQHL
PPLPPMQEES QDLGTRPALR QDTRHQSVDI SLPDHPALDT TPIPLHLNKH RQQISSRERQ
RESHAQPMRR RHDSSFTEQI APRRAVSSAK PNPKPSTRTV RRSLPASFDS SRAIPRTNQP
QNPEKSNSRE IQKWIARYES MGYPRQFVVE ALKRTTLTPG KSALLVMKHL SEGRDVPSHH
EGIWTDRDDA DLDFATSVDF HRSPADDSEE LQQERAQKAH NRLVNKHGFQ RFNLRKAFLE
AQAKEGGSHL EG
//
